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Monoclonal antibodies include an antigen-binding fragment (Fab) and a fragment crystallizable region (Fc). The Fab can bind to a tumor-associated antigen, while the Fc plays an important role in metabolic pathways, as well as in IgG-driven cellular functions.
The molecular sequence and subtype of antibodies will affect the effector functions. Such effector functions include the antibody dependent cellular cytotoxicity (ADCC) triggered by Fc binding to the FcγRIII receptor (CD16A) of NK. The Fc can also bind with serum complement molecules (C1q) to form a membrane attack complex (MAC) that triggers complement-dependent cytotoxicity (CDC). When Fc binds with macrophage receptors—namely FcγRIII (CD16A), FcγRII (CD32A) and FcγRI (CD64)—antibody-dependent cellular phagocytosis (ADCP) is triggered.
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FAQKilling tumors induced by mediated immune cells; Blocking dual target signal, exerting unique or repetitive functions, effectively preventing drug resistance; Greater specificity, targeting ability, and reduced off-target toxicity, effective reduction of treatment costs.
Bispecific antibodies (BsAbs), also known as bifunctional antibodies, can simultaneously recognize and bind two different antigens and epitopes, thereby blocking two different signaling pathways to exert their effects.
The preparation of bispecific antibodies mainly includes methods such as hybridoma fusion, chemical conjugation, recombinant gene preparation, etc. Recombinant DNA technology is currently the most used technology for preparing BsAb.
According to different structures, bispecific antibody structures can be divided into two main categories: bispecific antibodies with Fc fragment (IgG-like bispecific antibody) and bispecific antibodies without Fc fragment (non-IgG-like bispecific antibody).
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